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Thermodynamics of binding of divalent magnesium and manganese to uridine phosphates: implications for diabetes-related hypomagnesaemia and carbohydrate biocatalysis.

Authors
  • Zea, Corbin J
  • Camci-Unal, Gulden
  • Pohl, Nicola L
Type
Published Article
Journal
Chemistry Central journal
Publication Date
Jan 01, 2008
Volume
2
Pages
15–15
Identifiers
DOI: 10.1186/1752-153X-2-15
PMID: 18627619
Source
Medline
License
Unknown

Abstract

Our results indicate that the formal charge state of the phosphate containing substrates determine the binding strength. Divalent metal cations magnesium and manganese showed similar trends in binding to the sugar substrates. Enthalpy of binding values were all determined to be endothermic except for the PP(i) case. In addition, entropy of binding values were all found to be positive. From this data, we discuss the role of magnesium and manganese in both sugar nucleotidyltransferase and glycosyltransferase reactions, the differences in metal-bound substrates expected under normal physiological metal concentrations and those of hypomagnesaemia, and the implications for drug design.

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